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IID00860
UniprotQ96CF2
ProteinCharged multivesicular body protein 4c
GeneCHMP4C
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
233
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 216-233 Hetero dimer : IID00852Complex
 Evidence X-RAY 3c3r B Reference
       Region 3c3r B 221-233 order
 Evidence X-RAY 5v3r B Reference
       Region 5v3r B 216-220 disorder
       Region 5v3r B 221-233 order
 Evidence X-RAY 5wa1 B Reference
       Region 5wa1 B 216-220 disorder
       Region 5wa1 B 221-233 order
Seq 216-233 Hetero octamer : Q9H3S7
 Evidence X-RAY 5mk3 H Reference
       Region 5mk3 H 216-222 disorder
       Region 5mk3 H 223-233 order
 Evidence X-RAY 5mk3 G Reference
       Region 5mk3 G 216-223 disorder
       Region 5mk3 G 224-233 order
 Evidence X-RAY 5mk3 F Reference
       Region 5mk3 F 216-222 disorder
       Region 5mk3 F 223-233 order
 Evidence X-RAY 5mk3 E Reference
       Region 5mk3 E 216-222 disorder
       Region 5mk3 E 223-233 order
SeqProS possible 221-233 Same region of the homolog (Q9Y3E7, CHMP3) is disordered in the free state (PubMed=21827950). Hetero dimer : IID00852Complex
       Region 3c3r B 221-233 order
       Region 5v3r B 221-233 order
       Region 5wa1 B 221-233 order
SeqProS possible 223-233 Same region of the homolog (Q9Y3E7, CHMP3) is disordered in the free state (PubMed=21827950). Hetero octamer : Q9H3S7
       Region 5mk3 E 223-233 order
       Region 5mk3 F 223-233 order
       Region 5mk3 G 224-233 order
       Region 5mk3 H 223-233 order
Seqphosphorylation
    210-210 Phosphoserine; by AURKB
 
Prediction
NeProc
Disorder 1-21,153-233
Order 22-152
ProS 5-10,153-175,184-194,222-233
AlphaFold
Disorder 1-17,122-126,150-159,180-221,228-228,231-233
Order 18-121,127-149,160-179,222-227,229-230
Pfam Hmmer
PF03357 24-201 8.2e-73
SEG 2-16 ,62-74 ,157-176 ,204-218
Function
Function in SwissProt
Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: upon phosphorylation by AURKB, together with ZFYVE19/ANCHR, retains abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ANCHR and VPS4 and subsequent abscission (PubMed:22422861, PubMed:24814515). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413).
Biological Process
Diagram with PDB data
CHMP4C/PDCD6IPALIX BRO1 CHMP4C complex